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. 1969 Mar;62(3):644–649. doi: 10.1073/pnas.62.3.644

23Na NUCLEAR MAGNETIC RESONANCE RELAXATION STUDIES OF SODIUM ION INTERACTION WITH SOLUBLE RNA*

Thomas L James 1,†, Joseph H Noggle 1
PMCID: PMC223645  PMID: 5256995

Abstract

Interactions between 23Na+ and soluble RNA in aqueous solution are studied with the use of 23Na nuclear magnetic resonance. At low concentrations of NaCl, the interactions obey a simple equilibrium model with a formation constant log (Kf)3 = 2.8 ± 0.3. The relaxation rate of the bound sodium is found to be T1B-1 = 222 ± 19 sec-1 compared to that of free sodium T1F-1 = 17.5 sec-1. At high NaCl concentrations, the system deviates from the model, possibly owing to aggregation of the soluble RNA.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cope F. W. NMR evidence for complexing of Na+ in muscle, kidney, and brain, and by actomyosin. The relation of cellular complexing of Na+ to water structure and to transport kinetics. J Gen Physiol. 1967 May;50(5):1353–1375. doi: 10.1085/jgp.50.5.1353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Haugland R. P., Stryer L., Stengle T. R., Baldeschwieler J. D. Nuclear magnetic resonance studies of antibody-hapten interactions using a chloride ion probe. Biochemistry. 1967 Feb;6(2):498–502. doi: 10.1021/bi00854a018. [DOI] [PubMed] [Google Scholar]
  3. Rotunno C. A., Kowalewski V., Cereijido M. Nuclear spin resonance evidence for complexing of sodium in frog skin. Biochim Biophys Acta. 1967 Feb 1;135(1):170–173. doi: 10.1016/0005-2736(67)90022-3. [DOI] [PubMed] [Google Scholar]
  4. Smith I. C., Yamane T., Shulman R. G. Proton magnetic resonance of transfer RNA. Science. 1968 Mar 22;159(3821):1360–1361. doi: 10.1126/science.159.3821.1360. [DOI] [PubMed] [Google Scholar]
  5. Stengle T. R., Baldeschwieler J. D. Halide ions as chemical probes for NMR studies of proteins. Proc Natl Acad Sci U S A. 1966 May;55(5):1020–1025. doi: 10.1073/pnas.55.5.1020. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Stengle T. R., Baldeschwieler J. D. Halide ions as probes for nuclear magnetic resonance studies of proteins. The sulfhydryl groups of hemoglobin. J Am Chem Soc. 1967 Jun 7;89(12):3045–3050. doi: 10.1021/ja00988a044. [DOI] [PubMed] [Google Scholar]
  7. Ward R. L., Happe J. A. 35Cl NMR studies of zinc adenosine diphosphate complexes. Biochem Biophys Res Commun. 1967 Sep 7;28(5):785–790. doi: 10.1016/0006-291x(67)90386-5. [DOI] [PubMed] [Google Scholar]

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